| IED ID | IndEnz0018000990 |
| Enzyme Type ID | peroxidase000990 |
| Protein Name |
Glutathione S-transferase Mu 2 EC 2.5.1.18 GST 4-4 GSTM2-2 Glutathione S-transferase Yb-2 GST Yb2 |
| Gene Name | Gstm2 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MPMTLGYWDIRGLAHAIRLFLEYTDTSYEDKKYSMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLGRKHNLCGETEEERIRVDVLENQAMDTRLQLAMVCYSPDFERKKPEYLEGLPEKMKLYSEFLGKQPWFAGNKITYVDFLVYDVLDQHRIFEPKCLDAFPNLKDFVARFEGLKKISDYMKSGRFLSKPIFAKMAFWNPK |
| Enzyme Length | 218 |
| Uniprot Accession Number | P08010 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 50; /note=Glutathione; /evidence=ECO:0000305|PubMed:8664265; BINDING 116; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P28161};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000250|UniProtKB:P28161}; CATALYTIC ACTIVITY: Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate + glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925, ChEBI:CHEBI:132200, ChEBI:CHEBI:132201; Evidence={ECO:0000250|UniProtKB:P28161};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261; Evidence={ECO:0000250|UniProtKB:P28161}; |
| DNA Binding | |
| EC Number | 2.5.1.18 |
| Enzyme Function | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers. {ECO:0000250|UniProtKB:P28161}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (6); Binding site (2); Chain (1); Domain (2); Helix (8); Initiator methionine (1); Modified residue (3); Region (4); Sequence conflict (1); Turn (3) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Lipid metabolism;Olfaction;Phosphoprotein;Reference proteome;Sensory transduction;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 27; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 44; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 117; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P15626 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1B4P; |
| Mapped Pubmed ID | 10927022; 11015213; 11684093; 12027896; 12624007; 14646352; 16029322; 16396496; 17112229; 18008142; 19451092; 23470461; 8968379; |
| Motif | |
| Gene Encoded By | |
| Mass | 25,703 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16437; RHEA:16438; RHEA:50260; RHEA:50261 |
| Cross Reference Brenda |